Document Detail


A novel Ser O-glucuronidation in acidic proline-rich proteins identified by tandem mass spectrometry.
MedLine Citation:
PMID:  10858503     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human acidic proline-rich salivary protein PRP-1 and its C-terminally truncated form PRP-3 were analyzed by electrospray tandem mass spectrometry. Post-translational modifications were detected and characterized. A pyroglutamic acid residue was demonstrated at the N-terminus, Ser-8 and Ser-22 were shown to be phosphorylated and an O-linked glucuronic acid conjugation was identified. The latter modification was located to Ser-17 and found to be present in approximately 40% of the polypeptides.
Authors:
A P Jonsson; W J Griffiths; P Bratt; I Johansson; N Strömberg; H Jörnvall; T Bergman
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  475     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2000 Jun 
Date Detail:
Created Date:  2000-07-24     Completed Date:  2000-07-24     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  131-4     Citation Subset:  IM    
Affiliation:
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Chromatography, High Pressure Liquid
Glucuronic Acid / metabolism*
Humans
Mass Spectrometry / methods*
Molecular Sequence Data
Peptides / chemistry*,  isolation & purification,  metabolism
Proline / chemistry
Proline-Rich Protein Domains
Protein Processing, Post-Translational
Serine / metabolism*
Time Factors
Trypsin / metabolism
Chemical
Reg. No./Substance:
0/Peptides; 147-85-3/Proline; 56-45-1/Serine; 576-37-4/Glucuronic Acid; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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